Receptor tyrosine phosphatase, CD45 binds galectin-1 but does not mediate its apoptotic signal in T cell lines

Roberta Fajka-Boja, Marianna Szemes, Gabriela Ion, Ádám Légrádi, Michel Caron, Éva Monostori

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33 Citations (Scopus)


Galectin-1 (Gal-1) is an endogenous mammalian S-type lectin with highly pleiotropic effect on different tissues. The viability of the lymphoid cells is reduced by gal-1 by triggering apoptosis, however, the mechanism of the gal-1 induced apoptosis is still under investigation. The receptor tyrosine phosphatase, CD45, a heavily glycosylated cell surface molecule binds to gal-1 with high affinity, however, its contribution to the gal-1 induced apoptosis is still controversial. In this study we show that galectin-1 binds to cells deficient for CD45, although CD45 is one of the galectin-1-binding cell surface proteins on T cells. Moreover, the CD45 deficient Jurkat variant, J45.01 responds readily with tyrosine phosphorylation and subsequent apoptosis to galectin-1 treatment in a similar degree as its wild type counterpart, Jurkat does. These results strongly indicate that CD45 is not the receptor via gal-1 mediates the apoptotic signal into the cells as it was suggested in previous studies.

Original languageEnglish
Pages (from-to)149-154
Number of pages6
JournalImmunology letters
Issue number1-2
Publication statusPublished - Jun 3 2002



  • Apoptosis
  • CD45 tyrosine phosphatase
  • Galectin-1
  • Internalization
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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